ID G8YH24_PICSO Unreviewed; 630 AA.
AC G8YH24;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=glycerol kinase {ECO:0000256|ARBA:ARBA00012099};
DE EC=2.7.1.30 {ECO:0000256|ARBA:ARBA00012099};
DE AltName: Full=ATP:glycerol 3-phosphotransferase {ECO:0000256|ARBA:ARBA00043149};
GN Name=Piso0_003054 {ECO:0000313|EMBL:CCE80726.1};
GN ORFNames=GNLVRS01_PISO0G03878g {ECO:0000313|EMBL:CCE79961.1},
GN GNLVRS01_PISO0H03879g {ECO:0000313|EMBL:CCE80726.1};
OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS 10061 / NRRL Y-12695) (Hybrid yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE80726.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {ECO:0000313|EMBL:CCE80726.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000005222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005190}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family.
CC {ECO:0000256|ARBA:ARBA00009156, ECO:0000256|RuleBase:RU003733}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FO082053; CCE79961.1; -; Genomic_DNA.
DR EMBL; FO082052; CCE80726.1; -; Genomic_DNA.
DR AlphaFoldDB; G8YH24; -.
DR STRING; 559304.G8YH24; -.
DR eggNOG; KOG2517; Eukaryota.
DR HOGENOM; CLU_009281_2_2_1; -.
DR InParanoid; G8YH24; -.
DR UniPathway; UPA00618; UER00672.
DR Proteomes; UP000005222; Chromosome G.
DR Proteomes; UP000005222; Chromosome H.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004370; F:glycerol kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR InterPro; IPR018485; FGGY_C.
DR InterPro; IPR018484; FGGY_N.
DR InterPro; IPR005999; Glycerol_kin.
DR NCBIfam; TIGR01311; glycerol_kin; 1.
DR PANTHER; PTHR10196:SF69; GLYCEROL KINASE; 1.
DR PANTHER; PTHR10196; SUGAR KINASE; 1.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 3.
DR PROSITE; PS00933; FGGY_KINASES_1; 1.
DR PROSITE; PS00445; FGGY_KINASES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Kinase {ECO:0000256|RuleBase:RU003733};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000005222};
KW Transferase {ECO:0000256|RuleBase:RU003733}.
FT DOMAIN 94..348
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 357..569
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT REGION 41..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 69683 MW; A55CED228E73C543 CRC64;
MVRRQSNAPT HPLIASIDIG TTSARTILFD EHGTEIAKNQ IEYSTTASEA PADSKNKEQF
RRRSSLMRHN EPIFSAEGIA ISITDDVMIE NNAASVGPTL RYPKPGWVEC MPVHILANAV
QCLAASLITL RKINQNPALK IKYKVKAIGI ANMRETTIVW SRKTGKPLSN GITWTDTRTA
EIVQHLERMT DDEKKAELNQ KTGLPLSTYF SAAKLRWLLD NDDTIREEYE KGEGNLMFGT
VDTWLIYNMT KEKSFVSDVT NASRTYFMDL ETKDYDDELL EFWDIDPTRI CLPKIVSSSE
FYGSFATPNL SNLGFHNKIT PEAYEILKTL TGTPICGCLG DQSASLVGQL AFRPGSAKCT
YGTGCFLLYN TGIRKLISQH GALSTIGYWF PTLSEDDGKP HYALEGSIAV AGSIIQWLRD
NLKLIEQSKD VGPLASSVHD SGGVVFIPAF SGLYAPYWNS GARGTIFGMT QYTSASHIAR
AALEGVCFQV RSILKAMADD AGTSADFLEE ALNTQNESTP LATLAVDGGM SKADEVLQIQ
ADILGPCVTV KRAQISECTA LGAAIAAGLS FKDENERVWK DFNDVFEKID AANGNNSFKA
KLPDAERRRN WRRWERAIDR AKDWLDQNND
//
